FMO DATABASE

FMODB ID: 2LK1R

Calculation Name: 2FBN-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

Ligand 3-letter code:

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 2FBN

Chain ID: A

ChEMBL ID:

UniProt ID: Q8I4V8

Base Structure: X-ray

Registration Date: 2023-09-26

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptHSide
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422
Remarks

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	153
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1503751.599778
FMO2-HF: Nuclear repulsion	1441368.069322
FMO2-HF: Total energy	-62383.530456
FMO2-MP2: Total energy	-62567.015739

3D Structure Molmil

Snapshot

Ligand structure

Ligand Interaction

Ligand binding energy

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
N/A	N/A	N/A	N/A	N/A	N/A

Interactive mode: IFIE and PIEDA for fragment #1(A:22:ALA)

Summations of interaction energy for fragment #1(A:22:ALA)

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
1.81	3.759	0.097	-0.617	-1.429	0.002

Interaction energy analysis for fragmet #1(A:22:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : -0.023 / q_NPA : -0.022

Distance from base fragment(s) [Å]

Dist

Interaction energy by IFIE and PIEDA
[kcal/mol]

| Total | > | ES | > | EX | >
| CT+mix | > | DI(MP2) | >

Fragment charge [e]

FCHARGE q_Mulliken
q_NPA q(I=>J)

Residue

Res # RES

Sort

Graph Options

X Axis Label
Y Axis Max Y Axis Min
Display ES EX CT+mix DI(MP2)

frag_NumFragment number.	ChainChain species.	Res #Residue number.	RES3-letter code of amino acid residue, ligand and solvent molecule.	FCHARGEFormal charge [e].	q_MullikenFragment charge evaluated by Mulliken charge [e].	q_NPAFragment charge evaluated by natural population analysis(NPA) charge [e].	DISTDistance from Ligand [Å].	TotalIFIE at MP2 level [kcal/mol].	ESElectro static interaction energy by PIEDA [kcal/mol].	EXExchange-repulsion energy by PIEDA [kcal/mol].	CT+mixCharge transfer and mixing terms energy by PIEDA [kcal/mol].	DI(MP2)Dispersion energy by PIEDA [kcal/mol].	q(I=>J)Charge transfer value from I to J fragmens [e].
3	A	24	LYS	1	0.810	0.888	3.063	2.160	4.016	0.098	-0.614	-1.341	0.002
4	A	25	SER	0	-0.025	-0.010	5.241	0.453	0.546	-0.001	-0.003	-0.088	0.000
5	A	26	ILE	0	0.092	0.027	8.605	-0.077	-0.077	0.000	0.000	0.000	0.000
6	A	27	TYR	0	-0.013	-0.002	9.598	0.104	0.104	0.000	0.000	0.000	0.000
7	A	28	ASP	-1	-0.811	-0.885	5.732	-2.120	-2.120	0.000	0.000	0.000	0.000
8	A	29	TYR	0	-0.017	0.004	7.631	0.244	0.244	0.000	0.000	0.000	0.000
9	A	30	THR	0	0.019	-0.015	10.156	-0.049	-0.049	0.000	0.000	0.000	0.000
10	A	31	ASP	-1	-0.742	-0.881	12.891	0.022	0.022	0.000	0.000	0.000	0.000
11	A	32	GLU	-1	-0.833	-0.905	15.252	0.184	0.184	0.000	0.000	0.000	0.000
12	A	33	GLU	-1	-0.821	-0.892	8.854	0.906	0.906	0.000	0.000	0.000	0.000
13	A	34	LYS	1	0.821	0.930	12.671	0.048	0.048	0.000	0.000	0.000	0.000
14	A	35	VAL	0	-0.005	-0.002	14.149	-0.008	-0.008	0.000	0.000	0.000	0.000
15	A	36	GLN	0	-0.084	-0.046	13.594	-0.036	-0.036	0.000	0.000	0.000	0.000
16	A	37	SER	0	0.039	-0.001	10.931	0.033	0.033	0.000	0.000	0.000	0.000
17	A	38	ALA	0	0.009	0.019	12.979	-0.028	-0.028	0.000	0.000	0.000	0.000
18	A	39	PHE	0	-0.050	-0.036	16.186	-0.024	-0.024	0.000	0.000	0.000	0.000
19	A	40	ASP	-1	-0.820	-0.912	14.008	0.311	0.311	0.000	0.000	0.000	0.000
20	A	41	ILE	0	0.001	0.006	11.919	-0.016	-0.016	0.000	0.000	0.000	0.000
21	A	42	LYS	1	0.798	0.888	16.039	-0.127	-0.127	0.000	0.000	0.000	0.000
22	A	43	GLU	-1	-0.828	-0.897	19.133	0.096	0.096	0.000	0.000	0.000	0.000
23	A	44	GLU	-1	-0.817	-0.906	14.546	0.118	0.118	0.000	0.000	0.000	0.000
24	A	45	GLY	0	0.011	0.005	19.053	-0.014	-0.014	0.000	0.000	0.000	0.000
25	A	46	ASN	0	-0.040	-0.026	21.471	-0.019	-0.019	0.000	0.000	0.000	0.000
26	A	47	GLU	-1	-0.875	-0.940	21.723	0.081	0.081	0.000	0.000	0.000	0.000
27	A	48	PHE	0	-0.021	0.000	18.780	-0.006	-0.006	0.000	0.000	0.000	0.000
28	A	49	PHE	0	-0.027	-0.017	24.268	-0.009	-0.009	0.000	0.000	0.000	0.000
29	A	50	LYS	1	0.845	0.921	26.578	-0.076	-0.076	0.000	0.000	0.000	0.000
30	A	51	LYS	1	0.828	0.917	22.907	-0.065	-0.065	0.000	0.000	0.000	0.000
31	A	52	ASN	0	-0.060	-0.037	28.794	-0.005	-0.005	0.000	0.000	0.000	0.000
32	A	53	GLU	-1	-0.787	-0.867	25.143	0.040	0.040	0.000	0.000	0.000	0.000
33	A	54	ILE	0	-0.014	-0.020	25.817	0.001	0.001	0.000	0.000	0.000	0.000
34	A	55	ASN	0	-0.001	-0.005	26.017	-0.002	-0.002	0.000	0.000	0.000	0.000
35	A	56	GLU	-1	-0.823	-0.920	22.041	0.003	0.003	0.000	0.000	0.000	0.000
36	A	57	ALA	0	-0.005	-0.004	21.447	0.002	0.002	0.000	0.000	0.000	0.000
37	A	58	ILE	0	-0.065	-0.039	22.495	0.000	0.000	0.000	0.000	0.000	0.000
38	A	59	VAL	0	-0.002	0.004	18.125	-0.004	-0.004	0.000	0.000	0.000	0.000
39	A	60	LYS	1	0.813	0.914	14.016	-0.073	-0.073	0.000	0.000	0.000	0.000
40	A	61	TYR	0	-0.036	-0.063	18.522	0.000	0.000	0.000	0.000	0.000	0.000
41	A	62	LYS	1	0.848	0.919	20.677	0.025	0.025	0.000	0.000	0.000	0.000
42	A	63	GLU	-1	-0.771	-0.867	14.699	-0.013	-0.013	0.000	0.000	0.000	0.000
43	A	64	ALA	0	-0.041	-0.023	16.099	-0.003	-0.003	0.000	0.000	0.000	0.000
44	A	65	LEU	0	-0.063	-0.046	17.531	0.001	0.001	0.000	0.000	0.000	0.000
45	A	66	ASP	-1	-0.868	-0.935	16.330	-0.081	-0.081	0.000	0.000	0.000	0.000
46	A	67	PHE	0	-0.078	-0.041	10.503	-0.015	-0.015	0.000	0.000	0.000	0.000
47	A	68	PHE	0	-0.011	-0.019	15.915	0.011	0.011	0.000	0.000	0.000	0.000
48	A	69	ILE	0	-0.032	0.019	18.346	0.003	0.003	0.000	0.000	0.000	0.000
49	A	70	HIS	0	-0.031	-0.013	19.221	-0.001	-0.001	0.000	0.000	0.000	0.000
50	A	71	THR	0	0.007	0.000	19.188	0.005	0.005	0.000	0.000	0.000	0.000
51	A	72	GLU	-1	-0.947	-0.989	22.005	-0.029	-0.029	0.000	0.000	0.000	0.000
52	A	73	GLU	-1	-0.968	-0.983	24.856	-0.030	-0.030	0.000	0.000	0.000	0.000
53	A	74	TRP	0	-0.065	-0.030	17.932	0.012	0.012	0.000	0.000	0.000	0.000
54	A	75	ASP	-1	-0.892	-0.952	24.333	0.021	0.021	0.000	0.000	0.000	0.000
55	A	76	ASP	-1	-0.827	-0.902	23.243	0.091	0.091	0.000	0.000	0.000	0.000
56	A	77	GLN	0	-0.029	-0.026	25.325	0.001	0.001	0.000	0.000	0.000	0.000
57	A	78	ILE	0	-0.012	-0.004	23.832	0.002	0.002	0.000	0.000	0.000	0.000
58	A	79	LEU	0	-0.015	-0.015	19.387	0.008	0.008	0.000	0.000	0.000	0.000
59	A	80	LEU	0	0.012	0.015	22.763	-0.002	-0.002	0.000	0.000	0.000	0.000
60	A	81	ASP	-1	-0.862	-0.930	25.351	0.051	0.051	0.000	0.000	0.000	0.000
61	A	82	LYS	1	0.878	0.945	21.356	-0.136	-0.136	0.000	0.000	0.000	0.000
62	A	83	LYS	1	0.899	0.962	21.855	-0.004	-0.004	0.000	0.000	0.000	0.000
63	A	84	LYS	1	0.906	0.956	22.952	-0.037	-0.037	0.000	0.000	0.000	0.000
64	A	85	ASN	0	-0.082	-0.059	25.652	-0.007	-0.007	0.000	0.000	0.000	0.000
65	A	86	ILE	0	0.022	0.026	19.461	-0.004	-0.004	0.000	0.000	0.000	0.000
66	A	87	GLU	-1	-0.824	-0.918	23.330	0.007	0.007	0.000	0.000	0.000	0.000
67	A	88	ILE	0	-0.045	-0.017	24.887	-0.007	-0.007	0.000	0.000	0.000	0.000
68	A	89	SER	0	-0.048	-0.038	24.942	-0.003	-0.003	0.000	0.000	0.000	0.000
69	A	90	CYS	0	0.017	0.018	22.116	-0.001	-0.001	0.000	0.000	0.000	0.000
70	A	91	ASN	0	-0.020	-0.006	24.692	-0.011	-0.011	0.000	0.000	0.000	0.000
71	A	92	LEU	0	-0.011	-0.007	27.590	-0.004	-0.004	0.000	0.000	0.000	0.000
72	A	93	ASN	0	-0.029	-0.009	25.867	-0.006	-0.006	0.000	0.000	0.000	0.000
73	A	94	LEU	0	0.035	0.039	23.910	-0.003	-0.003	0.000	0.000	0.000	0.000
74	A	95	ALA	0	-0.005	0.004	27.918	-0.003	-0.003	0.000	0.000	0.000	0.000
75	A	96	THR	0	-0.045	-0.023	31.083	-0.002	-0.002	0.000	0.000	0.000	0.000
76	A	97	CYS	0	-0.019	0.005	27.946	0.000	0.000	0.000	0.000	0.000	0.000
77	A	98	TYR	0	0.052	0.020	26.894	-0.003	-0.003	0.000	0.000	0.000	0.000
78	A	99	ASN	0	-0.013	-0.018	32.062	-0.003	-0.003	0.000	0.000	0.000	0.000
79	A	100	LYS	1	0.892	0.965	32.493	-0.022	-0.022	0.000	0.000	0.000	0.000
80	A	101	ASN	0	-0.033	-0.033	30.062	0.002	0.002	0.000	0.000	0.000	0.000
81	A	102	LYS	1	0.878	0.956	34.039	-0.005	-0.005	0.000	0.000	0.000	0.000
82	A	103	ASP	-1	-0.794	-0.871	32.112	-0.019	-0.019	0.000	0.000	0.000	0.000
83	A	104	TYR	0	0.046	0.003	34.427	0.000	0.000	0.000	0.000	0.000	0.000
84	A	105	PRO	0	0.048	0.028	35.022	0.001	0.001	0.000	0.000	0.000	0.000
85	A	106	LYS	1	0.847	0.917	29.206	0.022	0.022	0.000	0.000	0.000	0.000
86	A	107	ALA	0	0.009	0.007	31.829	0.002	0.002	0.000	0.000	0.000	0.000
87	A	108	ILE	0	0.007	0.002	33.609	0.002	0.002	0.000	0.000	0.000	0.000
88	A	109	ASP	-1	-0.824	-0.875	29.743	-0.017	-0.017	0.000	0.000	0.000	0.000
89	A	110	HIS	0	0.026	-0.012	25.956	-0.002	-0.002	0.000	0.000	0.000	0.000
90	A	111	ALA	0	0.028	0.008	30.761	0.004	0.004	0.000	0.000	0.000	0.000
91	A	112	SER	0	-0.022	-0.040	33.696	0.002	0.002	0.000	0.000	0.000	0.000
92	A	113	LYS	1	0.790	0.871	27.458	0.021	0.021	0.000	0.000	0.000	0.000
93	A	114	VAL	0	0.025	0.026	30.254	0.002	0.002	0.000	0.000	0.000	0.000
94	A	115	LEU	0	-0.050	-0.020	31.977	0.002	0.002	0.000	0.000	0.000	0.000
95	A	116	LYS	1	0.872	0.941	32.513	0.007	0.007	0.000	0.000	0.000	0.000
96	A	117	ILE	0	0.041	0.041	28.103	0.000	0.000	0.000	0.000	0.000	0.000
97	A	118	ASP	-1	-0.831	-0.901	32.443	0.032	0.032	0.000	0.000	0.000	0.000
98	A	119	LYS	1	1.008	0.997	34.782	-0.007	-0.007	0.000	0.000	0.000	0.000
99	A	120	ASN	0	-0.022	-0.022	38.300	0.000	0.000	0.000	0.000	0.000	0.000
100	A	121	ASN	0	0.052	0.026	34.060	0.001	0.001	0.000	0.000	0.000	0.000
101	A	122	VAL	0	0.056	0.019	37.489	-0.002	-0.002	0.000	0.000	0.000	0.000
102	A	123	LYS	1	0.955	0.983	32.870	-0.040	-0.040	0.000	0.000	0.000	0.000
103	A	124	ALA	0	0.049	0.022	34.531	-0.002	-0.002	0.000	0.000	0.000	0.000
104	A	125	LEU	0	-0.009	0.006	36.108	-0.003	-0.003	0.000	0.000	0.000	0.000
105	A	126	TYR	0	-0.019	-0.002	38.768	-0.001	-0.001	0.000	0.000	0.000	0.000
106	A	127	LYS	1	0.867	0.923	33.485	-0.024	-0.024	0.000	0.000	0.000	0.000
107	A	128	LEU	0	0.021	0.012	37.338	-0.002	-0.002	0.000	0.000	0.000	0.000
108	A	129	GLY	0	0.027	0.008	38.565	-0.002	-0.002	0.000	0.000	0.000	0.000
109	A	130	VAL	0	-0.059	-0.032	39.647	-0.001	-0.001	0.000	0.000	0.000	0.000
110	A	131	ALA	0	0.018	0.011	37.421	-0.001	-0.001	0.000	0.000	0.000	0.000
111	A	132	ASN	0	0.009	-0.012	39.474	-0.003	-0.003	0.000	0.000	0.000	0.000
112	A	133	MET	0	-0.033	0.005	42.138	-0.001	-0.001	0.000	0.000	0.000	0.000
113	A	134	TYR	0	-0.089	-0.059	41.684	-0.001	-0.001	0.000	0.000	0.000	0.000
114	A	135	PHE	0	-0.015	-0.005	39.934	-0.001	-0.001	0.000	0.000	0.000	0.000
115	A	136	GLY	0	0.031	0.025	42.837	-0.001	-0.001	0.000	0.000	0.000	0.000
116	A	137	PHE	0	-0.039	0.005	41.024	0.000	0.000	0.000	0.000	0.000	0.000
117	A	138	LEU	0	0.013	-0.008	45.861	0.001	0.001	0.000	0.000	0.000	0.000
118	A	139	GLU	-1	-0.758	-0.865	48.613	0.000	0.000	0.000	0.000	0.000	0.000
119	A	140	GLU	-1	-0.837	-0.930	44.597	-0.003	-0.003	0.000	0.000	0.000	0.000
120	A	141	ALA	0	0.001	-0.003	44.704	0.001	0.001	0.000	0.000	0.000	0.000
121	A	142	LYS	1	0.946	0.958	45.704	-0.002	-0.002	0.000	0.000	0.000	0.000
122	A	143	GLU	-1	-0.914	-0.948	47.396	0.003	0.003	0.000	0.000	0.000	0.000
123	A	144	ASN	0	-0.057	-0.028	42.621	0.001	0.001	0.000	0.000	0.000	0.000
124	A	145	LEU	0	0.018	0.003	43.553	0.002	0.002	0.000	0.000	0.000	0.000
125	A	146	TYR	0	0.014	0.022	46.080	0.001	0.001	0.000	0.000	0.000	0.000
126	A	147	LYS	1	0.921	0.970	44.155	-0.008	-0.008	0.000	0.000	0.000	0.000
127	A	148	ALA	0	-0.001	-0.009	43.252	0.001	0.001	0.000	0.000	0.000	0.000
128	A	149	ALA	0	0.012	-0.011	44.798	0.002	0.002	0.000	0.000	0.000	0.000
129	A	150	SER	0	-0.045	-0.035	47.911	0.001	0.001	0.000	0.000	0.000	0.000
130	A	151	LEU	0	-0.068	-0.020	43.265	0.000	0.000	0.000	0.000	0.000	0.000
131	A	152	ASN	0	-0.013	-0.010	42.662	0.001	0.001	0.000	0.000	0.000	0.000
132	A	153	PRO	0	0.078	0.050	46.377	0.000	0.000	0.000	0.000	0.000	0.000
133	A	154	ASN	0	-0.003	-0.014	48.959	-0.002	-0.002	0.000	0.000	0.000	0.000
134	A	155	ASN	0	-0.043	-0.012	43.091	0.000	0.000	0.000	0.000	0.000	0.000
135	A	156	LEU	0	0.050	0.014	46.495	-0.001	-0.001	0.000	0.000	0.000	0.000
136	A	157	ASP	-1	-0.842	-0.903	42.598	0.020	0.020	0.000	0.000	0.000	0.000
137	A	158	ILE	0	-0.004	-0.008	42.298	-0.002	-0.002	0.000	0.000	0.000	0.000
138	A	159	ARG	1	0.898	0.950	45.304	-0.016	-0.016	0.000	0.000	0.000	0.000
139	A	160	ASN	0	0.014	0.000	47.256	-0.002	-0.002	0.000	0.000	0.000	0.000
140	A	161	SER	0	-0.020	-0.010	44.516	-0.001	-0.001	0.000	0.000	0.000	0.000
141	A	162	TYR	0	0.003	-0.002	46.704	-0.002	-0.002	0.000	0.000	0.000	0.000
142	A	163	GLU	-1	-0.887	-0.954	49.117	0.007	0.007	0.000	0.000	0.000	0.000
143	A	164	LEU	0	-0.039	-0.004	46.810	-0.001	-0.001	0.000	0.000	0.000	0.000
144	A	165	CYS	0	-0.009	-0.005	47.969	-0.001	-0.001	0.000	0.000	0.000	0.000
145	A	166	VAL	0	0.024	0.009	49.765	-0.001	-0.001	0.000	0.000	0.000	0.000
146	A	167	ASN	0	-0.088	-0.041	53.188	-0.001	-0.001	0.000	0.000	0.000	0.000
147	A	168	LYS	1	0.998	0.993	47.123	-0.002	-0.002	0.000	0.000	0.000	0.000
148	A	169	LEU	0	-0.022	0.005	52.272	-0.001	-0.001	0.000	0.000	0.000	0.000
149	A	170	LYS	1	0.912	0.945	53.850	-0.004	-0.004	0.000	0.000	0.000	0.000
150	A	171	GLU	-1	-0.875	-0.919	55.241	-0.001	-0.001	0.000	0.000	0.000	0.000
151	A	172	ALA	0	0.003	-0.006	53.404	-0.001	-0.001	0.000	0.000	0.000	0.000
152	A	173	ARG	1	0.809	0.885	55.272	0.000	0.000	0.000	0.000	0.000	0.000
153	A	174	LYS	1	0.790	0.909	58.256	0.000	0.000	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:22:ALA)